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Basic information

Entry
Database: PDB / ID: 1waz
TitleNMR Structure Determination of the bacterial mercury transporter, MerF, in micelles
ComponentsMERF
KeywordsTRANSPORT PROTEIN / PROTEIN STRUCTURE / RESIDUAL DIPOLAR COUPLING / POLYTOPIC MEMBRANE PROTEIN / ANTIBIOTIC RESISTANCE / MERCURY DETOXIFICATION
Function / homologybacterial mercury transporter, merf / Mercury ion transport, MerF / Membrane transport protein MerF / Helix Hairpins / Orthogonal Bundle / Mainly Alpha / membrane / MerF
Function and homology information
Biological speciesMORGANELLA MORGANII (bacteria)
MethodSOLUTION NMR / RESTRAINED MOLECULAR DYNAMICS
AuthorsHowell, S.C. / Mesleh, M.F. / Opella, S.J.
CitationJournal: Biochemistry / Year: 2005
Title: NMR Structure Determination of a Membrane Protein with Two Transmembrane Helices in Micelles: Merf of the Bacterial Mercury Detoxification System
Authors: Howell, S.C. / Mesleh, M.F. / Opella, S.J.
History
DepositionOct 28, 2004Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 11, 2005Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Apr 3, 2019Group: Data collection / Other / Source and taxonomy
Category: entity_src_gen / pdbx_database_proc ...entity_src_gen / pdbx_database_proc / pdbx_database_status / struct_biol
Item: _entity_src_gen.pdbx_host_org_cell_line / _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id ..._entity_src_gen.pdbx_host_org_cell_line / _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id / _entity_src_gen.pdbx_host_org_scientific_name / _entity_src_gen.pdbx_host_org_strain / _entity_src_gen.pdbx_host_org_variant / _pdbx_database_status.recvd_author_approval
Revision 1.4May 15, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_nmr_software
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_mr / _pdbx_nmr_software.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: MERF


Theoretical massNumber of molelcules
Total (without water)4,9461
Polymers4,9461
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)15 / 100LEAST RESTRAINT VIOLATION
Representative

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Components

#1: Protein/peptide MERF


Mass: 4945.946 Da / Num. of mol.: 1 / Fragment: HELIX-LOOP-HELIX CORE, RESIDUES 24-69
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) MORGANELLA MORGANII (bacteria) / Plasmid: PET31B/MERF / Production host: ESCHERICHIA COLI BL21(DE3) (bacteria) / Variant (production host): C43 / References: UniProt: Q56446
Sequence detailsFRAGMENT USED IN THIS EXPERIMENT COMPRISES RESIDUES 24-69

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D HNCA
1211H15N-HSQC
1312D- 1H15N-HMQC-NOESY
1411H15N- IPAP-HSQC
NMR detailsText: THE STRUCTURE WAS DETERMINED USING 1H-15N RESIDUAL DIPOLAR COUPLINGS FROM TWO NON-DEGENERATE ORIENTATIONS.

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Sample preparation

DetailsContents: 90% WATER/10% D20,500MM SDS, 10MM PHOSPHATE PH6.0, 0.7MM SAMPLE
Sample conditionspH: 6.0 / Pressure: 1.0 atm / Temperature: 333.0 K

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NMR measurement

NMR spectrometerType: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
Xplor-NIH2.9.4C.D.SCHWIETERS, J.J.KUSZEWSKI, N.TJrefinement
Xplor-NIHstructure solution
RefinementMethod: RESTRAINED MOLECULAR DYNAMICS / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE BIOCHEMISTRY CITATION ABOVE.
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 100 / Conformers submitted total number: 15

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